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Result: 1 - 7 of 7 rows are displayed

Reaction List for pathway PKA (Pathway Number 30) in Accession fig4_synapse (Accession Number 3)

Entries are grouped according to Pathway Number and they are alternately color coded using  and  color.
Further ordering can be done to the table header.  indicates that ordering is done according to ascending or descending order.
Keq is calculated only for first order reactions.
Kd is calculated only for second order reactions. [nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules]
  Reaction
Name		Pathway Name / 
Pathway No.		KfKbKdtauReagents
1 Release-C2PKA

Pathway No. 30		60
(s^-1)		18
(uM^-1 s^-1)		Kd(cb) = 0.3(uM)-  Substrate:
 R2C-cAMP4

 Products:
 PKA-active
 R2-cAMP4
2 Release-C1PKA

Pathway No. 30		60
(s^-1)		18
(uM^-1 s^-1)		Kd(cb) = 0.3(uM)-  Substrate:
 R2C2-cAMP4

 Products:
 PKA-active
 R2C-cAMP4
 The complex starts to dissociate and release catalytic subunit C. This has to be fast, as the activation of PKA by cAMP is also fast.
3 inhib-PKAPKA

Pathway No. 30		60
(uM^-1 s^-1)		1
(s^-1)		Kd(bf) = 0.0167(uM)-  Substrate:
 PKA-active
 PKA-inhibitor

 Products:
 inhibited-PKA
4 
  • cAMP-bind-site-B
    2
    		• PKA

    Pathway No. 30    		54
    (uM^-1 s^-1)    		33
    (s^-1)    		Kd(bf) = 0.6111(uM)-  Substrate:
     R2C2-cAMP
     cAMP

     Products:
     R2C2-cAMP2
     Kf = 54 /sec/uM, Kb = 33 /sec; Same Km (1e-07M) assumed as site B1.
    kf/kb = 0.7e-07M*1e06/(6e05^02) = 2e-13:2.77e-12
    5 
  • cAMP-bind-site-B
    1
    		• PKA

    Pathway No. 30    		54
    (uM^-1 s^-1)    		33
    (s^-1)    		Kd(bf) = 0.6111(uM)-  Substrate:
     R2C2
     cAMP

     Products:
     R2C2-cAMP
     Kf = 54 /sec/uM, Kb = 33 /sec; PKA in normal human T lymphocytes. Hasler et al (1992) FASEB J 6:2735-2741
    Kd =1e-07 M for type II, 5.6e-08 M for type I; Stephen B. Smith et al (1981) PNAS, USA 78: 1591-1595
    Ka1 = 2.1e+07 /M which gives Kd = 47 nM, Kan = 5e+08 /M or Kd of 2nM from Fig.7
    6 
  • cAMP-bind-site-A
    2
    		• PKA

    Pathway No. 30    		75
    (uM^-1 s^-1)    		32.5
    (s^-1)    		Kd(bf) = 0.4333(uM)-  Substrate:
     cAMP
     R2C2-cAMP3

     Products:
     R2C2-cAMP4
     Now cAMP shows effects of cooperativity and PKA has a low Kd for cAMP.
    7 
  • cAMP-bind-site-A
    1
    		• PKA

    Pathway No. 30    		75
    (uM^-1 s^-1)    		110
    (s^-1)    		Kd(bf) = 1.4667(uM)-  Substrate:
     R2C2-cAMP2
     cAMP

     Products:
     R2C2-cAMP3
     Kf = 75 /sec/uM, Kb = 110 /sec; This site has higher Kd for cAMP (kinetics within bovine myocardium)
    Dagfinn Ogreid and Stein Ove Doskeland (1981) FEBS Lett. 129(2):287-292
     
    Result: 1 - 7 of 7 rows are displayed


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